Stephen Henry Wright | |
---|---|
Born | |
Nationality | American |
Alma mater | University of California, Irvine |
Known for | solute transport mechanisms in kidney tubules |
Spouse(s) | Janis Mae Burt, Ph.D. |
Scientific career | |
Fields | Physiology |
Institutions | University of Arizona |
Thesis | Physiological characteristics of transport of amino acids in lamellibranch molluscs. |
Doctoral advisor | Grover C. Stephens |
Other academic advisors | John H. Crowe, Jared Diamond, Ernest M. Wright |
Stephen Henry Wright (born 1950) is an American physiologist. He is primarily known for his work on the mechanisms of organic solute transport in kidney tubules, but he is also known for work to describe transport of organic solutes across epithelial membranes by marine invertebrates. [1]
Stephen H. Wright was born 21 June 1950 in Alameda County, California. [2] He received bachelor's and master's degrees in biological sciences at the University of California, Davis studying in the laboratory John H. Crowe. He earned his Ph.D. in 1978 studying in the laboratory of Grover C. Stephens. For several years thereafter, he held post-doctoral positions at the University of California, Los Angeles in the laboratories of Jared Diamond and Ernest M. Wright studying ionic and organic solute transport mechanisms in intestinal and kidney tubule epithelia. On 18 July 1978 shortly after finishing graduate school at Irvine, he married biologist Janis Mae Burt, [3] [4] Both Wright and Burt joined the faculty of the University of Arizona. [5]
Wright joined faculty at the University of Arizona in 1982. While on the faculty of the University of Arizona he distinguished himself as a leading researcher in renal and transport physiology with three decades of funding by the National Institutes of Health, studying the renal transport of organic anions and cations at several different levels of biological organization. [1]
In cellular biology, active transport is the movement of molecules across a cell membrane from a region of lower concentration to a region of higher concentration—against the concentration gradient. Active transport requires cellular energy to achieve this movement. There are two types of active transport: primary active transport that uses adenosine triphosphate (ATP), and secondary active transport that uses an electrochemical gradient.
Cotransporters are a subcategory of membrane transport proteins (transporters) that couple the favorable movement of one molecule with its concentration gradient and unfavorable movement of another molecule against its concentration gradient. They enable cotransport and include antiporters and symporters. In general, cotransporters consist of two out of the three classes of integral membrane proteins known as transporters that move molecules and ions across biomembranes. Uniporters are also transporters but move only one type of molecule down its concentration gradient and are not classified as cotransporters.
Sodium-dependent glucose cotransporters are a family of glucose transporter found in the intestinal mucosa (enterocytes) of the small intestine (SGLT1) and the proximal tubule of the nephron. They contribute to renal glucose reabsorption. In the kidneys, 100% of the filtered glucose in the glomerulus has to be reabsorbed along the nephron. If the plasma glucose concentration is too high (hyperglycemia), glucose passes into the urine (glucosuria) because SGLT are saturated with the filtered glucose.
SLC22A5 is a membrane transport protein associated with primary carnitine deficiency. This protein is involved in the active cellular uptake of carnitine. It acts a symporter, moving sodium ions and other organic cations across the membrane along with carnitine. Such polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for the elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. Mutations in the SLC22A5 gene cause systemic primary carnitine deficiency, which can lead to heart failure.
The sulfate transporter is a solute carrier family protein that in humans is encoded by the SLC26A2 gene. SLC26A2 is also called the diastrophic dysplasia sulfate transporter (DTDST), and was first described by Hästbacka et al. in 1994. This sulfate (SO42−) transporter also accepts chloride, hydroxyl ions (OH−), and oxalate as substrates. SLC26A2 is expressed at high levels in developing and mature cartilage, as well as being expressed in lung, placenta, colon, kidney, pancreas and testis.
Multidrug resistance-associated protein 2 (MRP2) also called canalicular multispecific organic anion transporter 1 (cMOAT) or ATP-binding cassette sub-family C member 2 (ABCC2) is a protein that in humans is encoded by the ABCC2 gene.
Solute carrier family 22, member 4, also known as SLC22A4, is a human gene; the encoded protein is known as the ergothioneine transporter.
Solute carrier family 22 member 2 is a protein that in humans is encoded by the SLC22A2 gene.
Solute carrier family 22 member 1 is a protein that in humans is encoded by the gene SLC22A1.
Solute carrier family 22 member 3 (SLC22A3) also known as the organic cation transporter 3 (OCT3) or extraneuronal monoamine transporter (EMT) is a protein that in humans is encoded by the SLC22A3 gene.
Solute carrier family 22 member 11 is a protein that in humans is encoded by the SLC22A11 gene.
Solute carrier family 22 member 8, or organic anion transporter 3 (OAT3), is a protein that in humans is encoded by the SLC22A8 gene.
Solute carrier family 22, member 12, also known as SLC22A12 and URAT1, is a protein which in humans is encoded by the SLC22A12 gene.
The plasma membrane monoamine transporter (PMAT) is a low-affinity monoamine transporter protein which in humans is encoded by the SLC29A4 gene. It is known alternatively as the human equilibrative nucleoside transporter-4 (hENT4). Unlike other members of the ENT family, it is impermeable to most nucleosides, with the exception of the inhibitory neurotransmitter and ribonucleoside adenosine, which it is permeable to in a highly pH-dependent manner.
The organic anion transporter 1 (OAT1) also known as solute carrier family 22 member 6 (SLC22A6) is a protein that in humans is encoded by the SLC22A6 gene. It is a member of the organic anion transporter (OAT) family of proteins. OAT1 is a transmembrane protein that is expressed in the brain, the placenta, the eyes, smooth muscles, and the basolateral membrane of proximal tubular cells of the kidneys. It plays a central role in renal organic anion transport. Along with OAT3, OAT1 mediates the uptake of a wide range of relatively small and hydrophilic organic anions from plasma into the cytoplasm of the proximal tubular cells of the kidneys. From there, these substrates are transported into the lumen of the nephrons of the kidneys for excretion. OAT1 homologs have been identified in rats, mice, rabbits, pigs, flounders, and nematodes.
The proton-coupled folate transporter is a protein that in humans is encoded by the SLC46A1 gene. The major physiological roles of PCFTs are in mediating the intestinal absorption of folate, and its delivery to the central nervous system.
Members of the organic solute transporter (OST) family have been characterized from a small bottom feeding species of fish called the little skate, Raja erinacea. Members have also been characterized from humans and mice. The OST family is a member of the larger group of secondary carriers, the APC superfamily.
The anion exchanger family is a member of the large APC superfamily of secondary carriers. Members of the AE family are generally responsible for the transport of anions across cellular barriers, although their functions may vary. All of them exchange bicarbonate. Characterized protein members of the AE family are found in plants, animals, insects and yeast. Uncharacterized AE homologues may be present in bacteria. Animal AE proteins consist of homodimeric complexes of integral membrane proteins that vary in size from about 900 amino acyl residues to about 1250 residues. Their N-terminal hydrophilic domains may interact with cytoskeletal proteins and therefore play a cell structural role. Some of the currently characterized members of the AE family can be found in the Transporter Classification Database.
Members of the Organo Anion Transporter (OAT) Family are membrane transport proteins or 'transporters' that mediate the transport of mainly organic anions across the cell membrane. Therefore, OATPs are present in the lipid bilayer of the cell membrane, acting as the cell's gatekeepers. OATPs belong to the Solute Carrier Family (SLC) and the major facilitator superfamily.
Ernest Marshall Wright FRS is an Irish-born American physiologist. He is primarily known for his work on the mechanisms of glucose-sodium co-transporters in intestinal and other tissues in humans and animals.